Characterization of the Adhesive Properties of the Type IIb Subfamily Receptor Protein Tyrosine Phosphatases

Abstract

Receptor protein tyrosine phosphatases (RPTPs) have cell adhesion molecule–like extracellular domains coupled to cytoplasmic tyrosine phosphatase domains. PTPμ is the prototypical member of the type IIb subfamily of RPTPs, which includes PTPρ, PTPκ, and PCP-2. The authors performed the first comprehensive analysis of the subfamily in one system, examining adhesion and antibody recognition. The authors evaluated if antibodies that they developed to detect PTPmu also recognized other subfamily members. Notably, each antibody recognizes distinct subsets of type IIb RPTPs. PTPμ, PTPρ, and PTPκ have all been shown to mediate cell-cell aggregation, and prior work with PCP-2 indicated that it can mediate bead aggregation in vitro. This study reveals that PCP-2 is unique among the type IIb RPTPs in that it does not mediate cell-cell aggregation via homophilic binding. The authors conclude from these experiments that PCP-2 is likely to have a distinct biological function other than cell-cell aggregation.

Keywords::

• cell-cell aggregation
• cell adhesion
• homophilic binding
• receptor protein tyrosine phosphatase
• PCP-2
• tyrosine phosphatase

Declaration of interest: The authors report no conflicts of interest. The authors alone are responsible for the content and writing of the paper.